The first step of the vision process involves formation of the intermediate prelumirhodopsin within picoseconds of the absorption of light. Prelumirhodopsin is formed in high quantum yield and contains significant excess energy compared to its precursor, rhodopsin. We have developed theoretical approaches which enable us to simulate most of the experimental observations about the reactions of visual pigments, both in solution and embedded in proteins. We present three structural models for prelumirhodopsin ('two-acid cis', 'two-acid trans' and 'salt-bridge trans') and propose to compare experimental with calculated quantum yields and energy storage in order to distinguish between them using the following procedure: 1) We will calibrate the excited state potential surfaces of protonated Schiff bases of retinal (PSBR), using our semiclassical trajectories approach to reproduce rates and quantum yields of photoisomerization in solution. These potential surfaces will be combined with different constellations of charges embedded in a protein-like dielectric environment to understand roughly what electrostatic effects can increase the isomerization rate in solution by more than three orders of magnitude. 3) Our three models will be combined with optimum charge constellations and evaluated according to how well they simulate the formation rate, quantum yield and energy content prelumirhodopsin. Other proposed studies include simulation of the proton pump system of bacteriorhodopsin, calibration of the force field of PSBR's better to analyze the resonance Raman spectrum of prelumirhodopsin and synthesis of compounds which may be induced by light to store electrostatic energy.